Document Type

Journal Article

Date of this Version

9-10-2008

Publication Source

Journal of the American Chemical Society

Volume

130

Issue

36

Start Page

11921

Last Page

11927

DOI

10.1021/ja800697g

Abstract

We have developed a computational design strategy based on the alpha-helical coiled-coil to generate modular peptide motifs capable of assembling into metalloporphyrin arrays of varying lengths. The current study highlights the extension of a two-metalloporphyrin array to a four-metalloporphyrin array through the incorporation of a coiled-coil repeat unit. Molecular dynamics simulations demonstrate that the initial design evolves rapidly to a stable structure with a small rmsd compared to the original model. Biophysical characterization reveals elongated proteins of the desired length, correct cofactor stoichiometry, and cofactor specificity. The successful extension of the two-porphyrin array demonstrates how this methodology serves as a foundation to create linear assemblies of organized electrically and optically responsive cofactors.

Copyright/Permission Statement

This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of the American Chemical Society, copyright © American Chemical Society after peer review and technical editing by the publisher.

Keywords

Amino Acid Sequence, Circular Dichroism, Computer Simulation, Electron Spin Resonance Spectroscopy, Ferric Compounds, Metalloporphyrins, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Molecular Weight, Nanostructures, Peptides, Protein Structure, Secondary, Spectrophotometry, Ultraviolet, Thermodynamics

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Date Posted: 07 December 2016